Integrin and Extracellular Matrix

Host cell integrins are a family of heterodimeric transmembrane receptors, consisting of alpha and beta subunits, that mediate the attachment between a cell and its surrounding tissues, including other cells or the extracellular matrix (ECM) (Hynes, 2002; Takada et al., 2007). The ECM is a non-cellular structural network composed of proteins like collagen, laminin, and fibronectin that provides physical scaffolding and essential biochemical cues for cellular behavior (Frantz et al., 2010). Together, the integrin-ECM interaction acts as a bidirectional signaling hub, regulating vital processes such as cell survival, proliferation, and migration through mechanotransduction (Hynes, 2002; Frantz et al., 2010). In various diseases, this system is often hijacked; for instance, cancer cells utilize integrins to invade the ECM and metastasize, while many viruses and bacteria exploit these receptors as entry points into host cells (Hussein et al., 2015). Pharmacological targeting of this axis primarily involves monoclonal antibodies or small molecules designed to block specific integrin-ligand interactions, which has proven effective in treating inflammatory bowel disease, multiple sclerosis, and thrombotic disorders (Ley et al., 2016). However, therapeutic challenges remain, including the risk of systemic side effects like immunosuppression or impaired tissue repair due to the ubiquitous nature of these components (Ley et al., 2016).

Other names

Cell-matrix adhesion complexIntegrin-ECM axisAdhesion receptors and ligandsECM-receptor interaction

Antagonism of integrin-ligand binding to inhibit cell adhesion and downstream signaling pathways.